Analysis of introgressive lines of inter-species pea hybrids by band composition of seed proteins

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Abstract

Background. The reproductive incompatibility of cultivated (Pisum sativum) and wild (P. fulvum) pea species determines the difficulties of obtaining hybrids as well as the transfer of valuable wild parent alleles into interspecific hybrids and their use in the breeding process. The aim of the research was a comparative study of protein spectra of pea interspecific hybrids BC2F5 P. sativum × P. fulvum obtained by the authors and their parents.

Materials and methods. The band composition of seed proteins in the interspecific hybrids of peas BC2F5, variety Stabil (P. sativum) × accession from VIR collection I-609881 (P. fulvum) has been studied. Effectiveness of parent gene transfer determining each polymorphic position of electrophoretic spectrum were evaluated.

Results. The ratio of the actual frequencies of the bands of the cultivated and wild parents in the introgression lines corresponded to the expected level in 73% positions of the electrophoretic spectrum. The introgression rate of individual seed protein bands from wild parent into interspecific pea hybrids in the absence of selection significantly exceeded the expected level, which may indicate the adaptive value of alleles encoding unique seed protein isoforms.

Conclusion. The possibility of introgressive transfer of wild-type alleles to the cultivated genotypes of pea, as well as the presence of identified cultivated isoforms of storage proteins in all studied lines of BC2F5 interspecific hybrids in 88.2% of the polymorphic positions of the electrophoretic spectrum, indicates the possibility of using the wild species P. fulvum in pea breeding.

About the authors

Sergey V. Bobkov

Federal Scientific Center of Legumes and Groat Crops

Email: svbobkov@gmail.com
ORCID iD: 0000-0002-8146-0791

Candidate of Agricultural Sciences, Head of Laboratory, Plant Physiology and Biochemistry Laboratory

Russian Federation, Orel

Ivan A. Bychkov

Federal Scientific Center of Legumes and Groat Crops

Email: ivan.a.b@mail.ru

Junior Scientist, Plant Physiology and Biochemistry Laboratory

Russian Federation, Orel

Tatyana N. Selikhova

Federal Scientific Center of Legumes and Groat Crops

Email: tat.selihowa@yandex.ru

Candidate of Biological Sciences, Senior Scientist, Plant Physiology and Biochemistry Laboratory

Orel

Elena V. Semenova

Federal Research Center “N.I. Vavilov All-Russian Institute of Plant Genetic Resources”

Author for correspondence.
Email: e.semenova@vir.nw.ru
ORCID iD: 0000-0002-2637-1091

Candidate of Biological Sciences, Lead Scientist, Department of Legumes Genetic Resources

Russian Federation, Saint-Petersburg

Margarita A. Vishnyakova

Federal Research Center “N.I. Vavilov All-Russian Institute of Plant Genetic Resources”

Email: m.vishnyakova.vir@gmail.com
ORCID iD: 0000-0003-2808-7745

Doctor of Biological Sciences, Head of Department, Department of Legumes Genetic Resources

Russian Federation, Saint-Petersburg

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2. Fig. 1. Electrophoresic spectra of the seed proteins of parents and pea introgressive lines in hybrid combination Stabil x i-609881 (P. fulvum). Introgressive lines: 1 – А1; 2 – А2; 4 – А3; 5 – А4; 6 – А5; 7 – А6; 8 – А7; 9 – А8; 10 – А9; 11 – А10; 12 – А11; 13 – А12; 14 – А13. Parents: 15, 16 – i-609881 (P. fulvum); 17, 18 – variety Stabil. Proteins of soy beens variety Lantsetnaya are localized in spectrum 3

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3. Fig. 2. Electrophoresic spectra of seed proteins of variety Stabil: 1–3 – spectra obtained in the presence of mercaptoethanol, 4–9 – spectra without mercaptoethanol, 6 – soybean spectrum. Without mercaptoethanol, legumin is localized mostly at 60–65 kDa. In presence of mercaptoethanol the legumin molecules are dissociated into 2 subunits with molecular weights 35–46 and 21–23 kDa

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Copyright (c) 2020 Bobkov S.V., Bychkov I.A., Selikhova T.N., Semenova E.V., Vishnyakova M.A.

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This work is licensed under a Creative Commons Attribution 4.0 International License.
 


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